RIDA_CAPHI
ID RIDA_CAPHI Reviewed; 137 AA.
AC P80601; O97509;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=2-iminobutanoate/2-iminopropanoate deaminase {ECO:0000250|UniProtKB:P52758};
DE EC=3.5.99.10 {ECO:0000250|UniProtKB:P52758};
DE AltName: Full=14.3 kDa perchloric acid soluble protein {ECO:0000312|EMBL:AAC72281.1};
DE AltName: Full=Translation inhibitor L-PSP ribonuclease {ECO:0000250|UniProtKB:P52759};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P52759};
DE AltName: Full=UK114 antigen {ECO:0000303|PubMed:8814279};
GN Name=RIDA {ECO:0000250|UniProtKB:P52758};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-137, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=8814279; DOI=10.1016/0014-5793(96)00850-2;
RA Ceciliani F., Faotto L., Negri A., Colombo I., Berra B., Bartorelli A.,
RA Ronchi S.;
RT "The primary structure of UK114 tumor antigen.";
RL FEBS Lett. 393:147-150(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=9767104; DOI=10.1016/s0167-4781(98)00120-1;
RA Colombo I., Ceciliani F., Ronchi S., Bartorelli A., Berra B.;
RT "cDNA cloning and Escherichia coli expression of UK114 tumor antigen.";
RL Biochim. Biophys. Acta 1442:49-59(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 12-135, AND SUBUNIT.
RX PubMed=12925811; DOI=10.1107/s0907444903014306;
RA Deriu D., Briand C., Mistiniene E., Naktinis V., Grutter M.G.;
RT "Structure and oligomeric state of the mammalian tumour-associated antigen
RT UK114.";
RL Acta Crystallogr. D 59:1676-1678(2003).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of enamine/imine
CC intermediates that form during the course of normal metabolism. May
CC facilitate the release of ammonia from these potentially toxic reactive
CC metabolites, reducing their impact on cellular components. It may act
CC on enamine/imine intermediates formed by several types of pyridoxal-5'-
CC phosphate-dependent dehydratases including L-threonine dehydratase.
CC {ECO:0000250|UniProtKB:P52758}.
CC -!- FUNCTION: Also promotes endoribonucleolytic cleavage of some
CC transcripts by promoting recruitment of the ribonuclease P/MRP complex.
CC Acts by bridging YTHDF2 and the ribonuclease P/MRP complex. RIDA/HRSP12
CC binds to N6-methyladenosine (m6A)-containing mRNAs containing a 5'-
CC GGUUC-3' motif: cooperative binding of RIDA/HRSP12 and YTHDF2 to such
CC transcripts lead to recruitment of the ribonuclease P/MRP complex and
CC subsequent endoribonucleolytic cleavage.
CC {ECO:0000250|UniProtKB:P52758}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-iminobutanoate + H2O = 2-oxobutanoate + NH4(+);
CC Xref=Rhea:RHEA:39975, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:76545; EC=3.5.99.10;
CC Evidence={ECO:0000250|UniProtKB:P52758};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-iminopropanoate + H2O = NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:40671, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:44400; EC=3.5.99.10;
CC Evidence={ECO:0000250|UniProtKB:P52758};
CC -!- SUBUNIT: Homotrimer (PubMed:12925811). Interacts with YTHDF2 (By
CC similarity). {ECO:0000250|UniProtKB:P52758,
CC ECO:0000269|PubMed:12925811}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52758}. Nucleus
CC {ECO:0000250|UniProtKB:P52758}. Peroxisome
CC {ECO:0000250|UniProtKB:P52759}. Mitochondrion
CC {ECO:0000250|UniProtKB:P52759}. Note=Mostly cytoplasmic but, in less
CC differentiated cells occasionally nuclear.
CC {ECO:0000250|UniProtKB:P52758}.
CC -!- TISSUE SPECIFICITY: Expressed by various malignant neoplasms.
CC -!- MASS SPECTROMETRY: Mass=14206; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9767104};
CC -!- SIMILARITY: Belongs to the RutC family. {ECO:0000305}.
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DR EMBL; AF000167; AAC72281.1; -; mRNA.
DR PIR; S74181; S74181.
DR RefSeq; NP_001272642.1; NM_001285713.1.
DR PDB; 1NQ3; X-ray; 2.20 A; A/B/C/D/E/F=2-137.
DR PDBsum; 1NQ3; -.
DR AlphaFoldDB; P80601; -.
DR SMR; P80601; -.
DR STRING; 9925.ENSCHIP00000009683; -.
DR iPTMnet; P80601; -.
DR Ensembl; ENSCHIT00000017456; ENSCHIP00000009683; ENSCHIG00000012463.
DR GeneID; 100861379; -.
DR KEGG; chx:100861379; -.
DR CTD; 10247; -.
DR GeneTree; ENSGT00420000029792; -.
DR OMA; GSYFKEP; -.
DR OrthoDB; 1435276at2759; -.
DR EvolutionaryTrace; P80601; -.
DR Proteomes; UP000291000; Chromosome 14.
DR Bgee; ENSCHIG00000012463; Expressed in adult mammalian kidney and 17 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0120242; F:2-iminobutanoate deaminase activity; ISS:UniProtKB.
DR GO; GO:0120243; F:2-iminopropanoate deaminase activity; IEA:RHEA.
DR GO; GO:0016892; F:endoribonuclease activity, producing 3'-phosphomonoesters; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0061157; P:mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:1901565; P:organonitrogen compound catabolic process; ISS:UniProtKB.
DR Gene3D; 3.30.1330.40; -; 1.
DR InterPro; IPR006056; RidA.
DR InterPro; IPR019897; RidA_CS.
DR InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR006175; YjgF/YER057c/UK114.
DR PANTHER; PTHR11803; PTHR11803; 1.
DR Pfam; PF01042; Ribonuc_L-PSP; 1.
DR SUPFAM; SSF55298; SSF55298; 1.
DR TIGRFAMs; TIGR00004; TIGR00004; 1.
DR PROSITE; PS01094; UPF0076; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Lipid metabolism; Mitochondrion; Nucleus; Peroxisome; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9767104"
FT CHAIN 2..137
FT /note="2-iminobutanoate/2-iminopropanoate deaminase"
FT /id="PRO_0000170307"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9767104"
FT MOD_RES 13
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52760"
FT MOD_RES 67
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52760"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52758"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52758"
FT CONFLICT 3..11
FT /note="SLVRRIIST -> ENSEEPVGE (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="L -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1NQ3"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1NQ3"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:1NQ3"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1NQ3"
FT HELIX 51..67
FT /evidence="ECO:0007829|PDB:1NQ3"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1NQ3"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1NQ3"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:1NQ3"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1NQ3"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:1NQ3"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1NQ3"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1NQ3"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1NQ3"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:1NQ3"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1NQ3"
SQ SEQUENCE 137 AA; 14298 MW; DB59199B51EDABA0 CRC64;
MSSLVRRIIS TAKAPAAIGP YSQAVLVDRT IYISGQLGMD PASGQLVPGG VVEEAKQALT
NIGEILKAAG CDFTNVVKAT VLLADINDFS AVNDVYKQYF QSSFPARAAY QVAALPKGGR
VEIEAIAVQG PLTTASL
